(data stored in SCRATCH zone)

SWISSPROT: B1K365_BURCC

ID   B1K365_BURCC            Unreviewed;       290 AA.
AC   B1K365;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN   OrderedLocusNames=Bcenmc03_3567 {ECO:0000313|EMBL:ACA92719.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92719.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
CC       complex. Biotin carboxylase (BC) catalyzes the carboxylation of
CC       biotin on its carrier protein (BCCP) and then the CO(2) group is
CC       transferred by the transcarboxylase to acetyl-CoA to form malonyl-
CC       CoA. {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS01143984}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] =
CC         malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-
CC         COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01395,
CC         ECO:0000256|SAAS:SAAS01143883};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS01143898}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
CC       biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
CC       and two subunits each of ACCase subunit alpha (AccA) and ACCase
CC       subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS01146252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
CC       ECO:0000256|SAAS:SAAS01146251}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01395, ECO:0000256|SAAS:SAAS01143894}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000959; ACA92719.1; -; Genomic_DNA.
DR   RefSeq; WP_009691548.1; NC_010515.1.
DR   EnsemblBacteria; ACA92719; ACA92719; Bcenmc03_3567.
DR   KEGG; bcm:Bcenmc03_3567; -.
DR   HOGENOM; HOG000021670; -.
DR   KO; K01963; -.
DR   OMA; PEGLWIK; -.
DR   BioCyc; BCEN406425:G1GBC-3788-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000002169; Chromosome 2.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR041010; Znf-ACC.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF17848; zf-ACC; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1K365.
DR   SWISS-2DPAGE; B1K365.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143850};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01146259};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143881};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143991};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143978};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143853};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01146243};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143831};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01143821, ECO:0000313|EMBL:ACA92719.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01395, ECO:0000256|SAAS:SAAS01146260};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395,
KW   ECO:0000256|SAAS:SAAS01146249}.
FT   DOMAIN       27    290       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   ZN_FING      31     53       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_01395}.
FT   METAL        31     31       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        34     34       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        50     50       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   METAL        53     53       Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
SQ   SEQUENCE   290 AA;  31877 MW;  0A1C3C2D27618564 CRC64;
     MSWLDKLLPP KIKQTDPKSR KGIPEGLWVK CPSCEAVLYR NDVDANLHVC PKCDHHMRIG
     ARERLDGLLD PEGRYEIGQE IVPVDSLKFK DSRKYPDRLK EAMDETGETD AMVVMGGAIH
     TLPVVAACFE FSFMGGSMGS VVGERFARGA QNALEQHVPF ICFTASGGAR MQESLLSLMQ
     MAKTTAMLTK LAEAKLPFIS VLTDPTMGGV SASFAFLGDV VIAEPKALIG FAGPRVIEQT
     VREKLPEGFQ RAEFLLKTGA IDMIVDRRKM RDEIAQLLAL LQRQPADALA
//

If you have problems or comments...

PBIL Back to PBIL home page